Datasheet |
|
Target Protein |
ENPP1 |
Clonality |
Polyclonal |
Storage/Stability |
-20°C/1 year |
Application |
WB,ELISA |
Recommended Dilution |
WB 1:500-2000 ELISA 1:5000-20000 |
Concentration |
1 mg/ml |
Reactive Species |
Human,Mouse,Rat |
Host Species |
Rabbit |
Immunogen |
Synthesized peptide derived from part region of human protein |
Specificity |
ENPP1 Polyclonal Antibody detects endogenous levels of protein. |
Purification |
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen |
Form |
Liquid in PBS containing 50% glycerol, and 0.02% sodium azide. |
Gene Name |
ENPP1 M6S1 NPPS PC1 PDNP1 |
Accession No. |
P22413 P06802 Q924C3 |
Description |
ectonucleotide pyrophosphatase/phosphodiesterase 1(ENPP1) Homo sapiens This gene is a member of the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP) family. The encoded protein is a type II transmembrane glycoprotein comprising two identical disulfide-bonded subunits. This protein has broad specificity and cleaves a variety of substrates, including phosphodiester bonds of nucleotides and nucleotide sugars and pyrophosphate bonds of nucleotides and nucleotide sugars. This protein may function to hydrolyze nucleoside 5' triphosphates to their corresponding monophosphates and may also hydrolyze diadenosine polyphosphates. Mutations in this gene have been associated with 'idiopathic' infantile arterial calcification, ossification of the posterior longitudinal ligament of the spine (OPLL), and insulin resistance. [provided by RefSeq, Jul 2008], |
Cell Pathway/ Category |
Purine metabolism,Starch and sucrose metabolism,Riboflavin metabolism,Nicotinate and nicotinamide metabolism,Pantothenate and CoA biosynthesis, |
Protein Expression |
Human rectum tumor,Liver,Placenta,Skin,Skin fibrobl |
Subcellular Localization |
extracellular space,lysosomal membrane,plasma membrane,integral component of plasma membrane,cell surface,integral component of membrane,basolateral plasma membrane, |
Protein Function |
catalytic activity:A dinucleotide + H(2)O = 2 mononucleotides.,catalytic activity:Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.,caution:It is uncertain whether Met-1 or Met-53 is the initiator.,cofactor:Binds 2 divalent metal cations per subunit.,disease:Defects in ENPP1 are a cause of idiopathic infantile arterial calcification (IIAC) [MIM:208000]; also called generalized arterial calcification of infancy. IIAC is characterized by calcification of the internal elastic lamina of muscular arteries and stenosis due to myointimal proliferation.,disease:Defects in ENPP1 are a cause of increased susceptibility for ossification of the posterior longitudinal ligament of the spine (OPLL) [MIM:602475]. OPLL is a common form of human myelopathy with a prevalence of as much as 4% in a variety of ethnic groups.,disease:Defects in ENPP1 are associated with obesity, glucose intolerance, and type II diabetes non-insulin dependent (NIDDM) [MIM:125853].,domain:The di-leucine motif is required for basolateral targeting in epithelial cells, and for targeting to matrix vesicles derived from mineralizing cells.,enzyme regulation:At low concentrations of ATP, a phosphorylated intermediate is formed which inhibits further hydrolysis.,function:Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity.,PTM:Autophosphorylated as part of the catalytic cycle of phosphodiesterase/pyrophosphatase activity.,PTM:It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.,PTM:N-glycosylated.,similarity:Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.,similarity:Contains 2 SMB (somatomedin-B) domains.,subcellular location:Targeted to the basolateral membrane in polarized epithelial cells and in hepatocytes, and to matrix vesicles in osteoblasts. In bile duct cells and cancer cells, located to the apical cytoplasmic side.,subunit:Homodimer; disulfide-linked.,tissue specificity:Expressed in plasma cells and also in a number of non-lymphoid tissues, including the distal convoluted tubule of the kidney, chondrocytes and epididymis., |
Usage |
For Research Use Only! Not for diagnostic or therapeutic procedures. |